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Conserved domains on  [gi|298566312|ref|NP_001177312|]
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bifunctional UDP-N-acetylglucosamine 2-epimerase/N-acetylmannosamine kinase isoform 4 [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
NeuC_NnaA super family cl40678
UDP-N-acetyl-D-glucosamine 2-epimerase, UDP-hydrolysing; This family of enzymes catalyzes the ...
 11-374 3.21e-129

UDP-N-acetyl-D-glucosamine 2-epimerase, UDP-hydrolysing; This family of enzymes catalyzes the combined epimerization and UDP-hydrolysis of UDP-N-acetylglucosamine to N-acetylmannosamine. This is in contrast to the related enzyme WecB (TIGR00236) which retains the UDP moiety. NeuC acts in concert with NeuA and NeuB to synthesize CMP-N5-acetyl-neuraminate.


The actual alignment was detected with superfamily member TIGR03568:

Pssm-ID: 274654  Cd Length: 364  Bit Score: 384.96  E-value: 3.21e-129
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298566312   11 RVCVATCNRADYSKLAPIMFGIKTEPEFfELDVVVLGSHLIDDYGNTYRMIEQDDFDINTRLHTIVRGEDEAAMVESVGL 90
Cdd:TIGR03568   1 KICVVTGTRADYGLLRPLLKALQDDPDL-ELQLIVTGMHLSPEYGNTVNEIEKDGFDIDEKIEILLDSDSNAGMAKSMGL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298566312   91 ALVKLPDVLNRLKPDIMIVHGDRFDALALATSAALMNIRILHIEGGEVS-GTIDDSIRHAITKLAHYHVCCTRSAEQHLI 169
Cdd:TIGR03568  80 TIIGFSDAFERLKPDLVVVLGDRFEMLAAAIAAALLNIPIAHIHGGEVTeGAIDESIRHAITKLSHLHFVATEEYRQRVI 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298566312  170 SMCEDHDRILLAGCPSYDKLlsaKNKDYMS--IIRMWLGDDvKSKDYIVALQHPVTTDIKHSIKMFELTLDALISFNKRT 247
Cdd:TIGR03568 160 QMGEDPDRVFNVGSPGLDNI---LSLDLLSkeELEEKLGID-LDKPYALVTFHPVTLEKAEAEEQIKELLKALDELNKNI 235

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298566312  248 LVLFPNIDAGSKEMVRVMRKKgIEHHPNFRAVKHVPFDQFIQLVAHAGCMIGNSSCGVREVGAFGTPVINLGTRQIGRET 327
Cdd:TIGR03568 236 IFTYPNADAGSRIINEAIEEY-VEKHPNFRLFKSLGQERYLSLLKNADAVIGNSSSGIIEAPSFGVPTINIGTRQKGRLR 314

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|..
gi 298566312  328 GENVLHVrDADTQDkILQALHLQFGKQYPCSK-----IYGDGNAVPRILKFL 374
Cdd:TIGR03568 315 ADSVIDV-DPDKEE-IVKAIEKALDPAFKKSLkkvknPYGDGNSSKRIIEIL 364
ASKHA_ATPase-like super family cl49607
ATPase-like domain of the ASKHA (Acetate and Sugar Kinases/Hsc70/Actin) superfamily; The ASKHA ...
 408-638 7.78e-126

ATPase-like domain of the ASKHA (Acetate and Sugar Kinases/Hsc70/Actin) superfamily; The ASKHA superfamily, also known as actin-like ATPase domain superfamily, includes acetate and sugar kinases, heat-shock cognate 70 (Hsp70) and actin family proteins. They either function as conformational hydrolases (e.g. Hsp70, actin) that perform simple ATP hydrolysis, or as metabolite kinases (e.g. glycerol kinase) that catalyze the transfer of a phosphoryl group from ATP to their cognate substrates. Both activities depend on the presence of specific metal cations. ASKHA superfamily members share a common core fold that includes an actin-like ATPase domain consisting of two subdomains (denoted I _ II) with highly similar ribonuclease (RNase) H-like folds. The fold of each subdomain is characterized by a central five strand beta-sheet and flanking alpha-helices. The two subdomains form an active site cleft in which ATP binds at the bottom. Another common feature of ASKHA superfamily members is the coupling of phosphoryl-group transfer to conformational rearrangement, leading to domain closure. Substrate binding triggers protein motion.


The actual alignment was detected with superfamily member cd24060:

Pssm-ID: 483947 [Multi-domain]  Cd Length: 305  Bit Score: 374.06  E-value: 7.78e-126
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298566312 408 SALAVDLGGTNLRVAIVSMKGEIVKKYTQFNPKTYEERINLILQMCVEAAAEAVKLNCRILGVGIGGG------------ 475
Cdd:cd24060    1 SALAVDLGGTNLRVAIVSMKGEIVKKYTQPNPKTYEERIDLILQMCVEAASEAVKLNCRILGVGISTGgrvnpregivlh 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298566312 476 --------------------------------------------------------------IIHQHELIHGSSFCAAEL 493
Cdd:cd24060   81 stkliqewssvdlrtpisdalhlpvwvdndgncaalaerkfghgkgvenfvtvitgtgigggIILNHELIHGSSFCAAEL 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298566312 494 GHLVVSLDGPDCSCGSHGCIEAYASGMALQREAKKLHDEDLLLVEGMSVPKDEAVGALHLIQAAKLGNAKAQSILRTAGT 573
Cdd:cd24060  161 GHIVVSLDGPDCMCGSHGCVEAYASGMALQREAKKLHDEDLLLVEGMSVTNDEEVTAKHLIQAAKLGNAKAQKILRTAGT 240

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 298566312 574 ALGLGVVNILHTMNPSLVILSGVLASHYIHIVKDVIRQQALSSVQDVDVVVSDLVDPALLGAASM 638
Cdd:cd24060  241 ALGLGIVNILHTLNPSLVILSGVLASHYENIVKDVIAQRALPSVQNVDVVVSDLVDPALLGAASM 305
 
Name Accession Description Interval E-value
NeuC_NnaA TIGR03568
UDP-N-acetyl-D-glucosamine 2-epimerase, UDP-hydrolysing; This family of enzymes catalyzes the ...
 11-374 3.21e-129

UDP-N-acetyl-D-glucosamine 2-epimerase, UDP-hydrolysing; This family of enzymes catalyzes the combined epimerization and UDP-hydrolysis of UDP-N-acetylglucosamine to N-acetylmannosamine. This is in contrast to the related enzyme WecB (TIGR00236) which retains the UDP moiety. NeuC acts in concert with NeuA and NeuB to synthesize CMP-N5-acetyl-neuraminate.


Pssm-ID: 274654  Cd Length: 364  Bit Score: 384.96  E-value: 3.21e-129
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298566312   11 RVCVATCNRADYSKLAPIMFGIKTEPEFfELDVVVLGSHLIDDYGNTYRMIEQDDFDINTRLHTIVRGEDEAAMVESVGL 90
Cdd:TIGR03568   1 KICVVTGTRADYGLLRPLLKALQDDPDL-ELQLIVTGMHLSPEYGNTVNEIEKDGFDIDEKIEILLDSDSNAGMAKSMGL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298566312   91 ALVKLPDVLNRLKPDIMIVHGDRFDALALATSAALMNIRILHIEGGEVS-GTIDDSIRHAITKLAHYHVCCTRSAEQHLI 169
Cdd:TIGR03568  80 TIIGFSDAFERLKPDLVVVLGDRFEMLAAAIAAALLNIPIAHIHGGEVTeGAIDESIRHAITKLSHLHFVATEEYRQRVI 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298566312  170 SMCEDHDRILLAGCPSYDKLlsaKNKDYMS--IIRMWLGDDvKSKDYIVALQHPVTTDIKHSIKMFELTLDALISFNKRT 247
Cdd:TIGR03568 160 QMGEDPDRVFNVGSPGLDNI---LSLDLLSkeELEEKLGID-LDKPYALVTFHPVTLEKAEAEEQIKELLKALDELNKNI 235

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298566312  248 LVLFPNIDAGSKEMVRVMRKKgIEHHPNFRAVKHVPFDQFIQLVAHAGCMIGNSSCGVREVGAFGTPVINLGTRQIGRET 327
Cdd:TIGR03568 236 IFTYPNADAGSRIINEAIEEY-VEKHPNFRLFKSLGQERYLSLLKNADAVIGNSSSGIIEAPSFGVPTINIGTRQKGRLR 314

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|..
gi 298566312  328 GENVLHVrDADTQDkILQALHLQFGKQYPCSK-----IYGDGNAVPRILKFL 374
Cdd:TIGR03568 315 ADSVIDV-DPDKEE-IVKAIEKALDPAFKKSLkkvknPYGDGNSSKRIIEIL 364
ASKHA_NBD_ROK_GNE cd24060
nucleotide-binding domain (NBD) of bifunctional UDP-N-acetylglucosamine 2-epimerase ...
 408-638 7.78e-126

nucleotide-binding domain (NBD) of bifunctional UDP-N-acetylglucosamine 2-epimerase/N-acetylmannosamine kinase (GNE) and similar proteins; GNE (EC 3.2.1.183/EC 2.7.1.60), also called UDP-GlcNAc-2-epimerase/ManAc kinase, is a bi-functional enzyme that plays a key role in sialic acid biosynthesis. It regulates and initiates biosynthesis of N-acetylneuraminic acid (NeuAc), a precursor of sialic acids. It plays an essential role in early development and required for normal sialylation in hematopoietic cells. Sialylation is implicated in cell adhesion, signal transduction, tumorigenicity and metastatic behavior of malignant cells. GNE is the only human protein that contains a kinase domain belonging to the ROK (repressor, ORF, kinase) family. Mutations of the GNE protein cause sialurea or autosomal recessive inclusion body myopathy/Nonaka myopathy.


Pssm-ID: 466910 [Multi-domain]  Cd Length: 305  Bit Score: 374.06  E-value: 7.78e-126
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298566312 408 SALAVDLGGTNLRVAIVSMKGEIVKKYTQFNPKTYEERINLILQMCVEAAAEAVKLNCRILGVGIGGG------------ 475
Cdd:cd24060    1 SALAVDLGGTNLRVAIVSMKGEIVKKYTQPNPKTYEERIDLILQMCVEAASEAVKLNCRILGVGISTGgrvnpregivlh 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298566312 476 --------------------------------------------------------------IIHQHELIHGSSFCAAEL 493
Cdd:cd24060   81 stkliqewssvdlrtpisdalhlpvwvdndgncaalaerkfghgkgvenfvtvitgtgigggIILNHELIHGSSFCAAEL 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298566312 494 GHLVVSLDGPDCSCGSHGCIEAYASGMALQREAKKLHDEDLLLVEGMSVPKDEAVGALHLIQAAKLGNAKAQSILRTAGT 573
Cdd:cd24060  161 GHIVVSLDGPDCMCGSHGCVEAYASGMALQREAKKLHDEDLLLVEGMSVTNDEEVTAKHLIQAAKLGNAKAQKILRTAGT 240

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 298566312 574 ALGLGVVNILHTMNPSLVILSGVLASHYIHIVKDVIRQQALSSVQDVDVVVSDLVDPALLGAASM 638
Cdd:cd24060  241 ALGLGIVNILHTLNPSLVILSGVLASHYENIVKDVIAQRALPSVQNVDVVVSDLVDPALLGAASM 305
GTB_UDP-GlcNAc_2-Epimerase cd03786
UDP-N-acetylglucosamine 2-epimerase and similar proteins; Bacterial members of the ...
 11-375 2.81e-103

UDP-N-acetylglucosamine 2-epimerase and similar proteins; Bacterial members of the UDP-N-Acetylglucosamine (GlcNAc) 2-Epimerase family (EC 5.1.3.14) are known to catalyze the reversible interconversion of UDP-GlcNAc and UDP-N-acetylmannosamine (UDP-ManNAc). The enzyme serves to produce an activated form of ManNAc residues (UDP-ManNAc) for use in the biosynthesis of a variety of cell surface polysaccharides; The mammalian enzyme is bifunctional, catalyzing both the inversion of stereochemistry at C-2 and the hydrolysis of the UDP-sugar linkage to generate free ManNAc. It also catalyzes the phosphorylation of ManNAc to generate ManNAc 6-phosphate, a precursor to salic acids. In mammals, sialic acids are found at the termini of oligosaccharides in a large variety of cell surface glycoconjugates and are key mediators of cell-cell recognition events. Mutations in human members of this family have been associated with Sialuria, a rare disease caused by the disorders of sialic acid metabolism. This family belongs to the GT-B structural superfamily of glycoslytransferases, which have characteristic N- and C-terminal domains each containing a typical Rossmann fold. The two domains have high structural homology despite minimal sequence homology. The large cleft that separates the two domains includes the catalytic center and permits a high degree of flexibility.


Pssm-ID: 340819 [Multi-domain]  Cd Length: 365  Bit Score: 318.38  E-value: 2.81e-103
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298566312  11 RVCVATCNRADYSKLAPIMFGIKTEPEFfELDVVVLGSHLIDDYGNTYRMIEqddFDINTRLHTIVRGEDEAAMVESVGL 90
Cdd:cd03786    1 KILTVTGTRPEAIKLAPVLRALKKDPGL-ELVLVVTGQHLDMLLGVLFFFIL---FLIKPDYDLDLMGDNQTLGAKTGGL 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298566312  91 aLVKLPDVLNRLKPDIMIVHGDRFDALALATSAALMNIRILHIEGGEVS---GTIDDSIRHAITKLAHYHVCCTRSAEQH 167
Cdd:cd03786   77 -LIGLEEVLFEEKPDAVLVLGDTNTTLAGALAAFKLGIPVAHVEAGLRSfdlGMPEEENRHRIDKLSDLHFAPTEEAREN 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298566312 168 LISMCEDHDRILLAGCPSYDKLLSAKNKDYMSIIrmWLGDDVKSKDYIVALQHPVTTDikHSIKMFELTLDALISFNKR- 246
Cdd:cd03786  156 LLQEGEPPERIFVTGNTVIDALLSAALRIRDELV--LSKLGLLEKKYILVTLHRRENV--DSGERLEELLEALEELAEKy 231

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298566312 247 -TLVLFPNIDAGSKEMVRVMRKKgIEHHPNFRAVKHVPFDQFIQLVAHAGCMIGNSScGVREVGAF-GTPVINLGTRQIG 324
Cdd:cd03786  232 dLIVVYPNHPRTRPRIREVGLKF-LGGLPNIRLIDPLGYLDLVLLKKRAKLVLTDSG-GIQEEASFlGKPVLVLRDRTER 309

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 298566312 325 RETGENVLHVRDADTQDKILQALHLQFGKQYPCSK-----IYGDGNAVPRILKFLK 375
Cdd:cd03786  310 PERVEAGTNVLVGTDPEAILEAIEKLLSDEFEYSRmsainPYGDGNASERIVDILE 365
Epimerase_2 pfam02350
UDP-N-acetylglucosamine 2-epimerase; This family consists of UDP-N-acetylglucosamine ...
 37-375 2.77e-61

UDP-N-acetylglucosamine 2-epimerase; This family consists of UDP-N-acetylglucosamine 2-epimerases EC:5.1.3.14 this enzyme catalyzes the production of UDP-ManNAc from UDP-GlcNAc. Note that some of the enzymes is this family are bifunctional such as Swiss:O35826 and Swiss:Q9Z0P6 in this instance Pfam matches only the N-terminal half of the protein suggesting that the additional C-terminal part (when compared to mono-functional members of this family) is responsible for the UPD-N-acetylmannosamine kinase activity of these enzymes. This hypothesis is further supported by the assumption that the C-terminal part of Swiss:O35826 is the kinase domain.


Pssm-ID: 426733 [Multi-domain]  Cd Length: 336  Bit Score: 207.39  E-value: 2.77e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298566312   37 EFFELDVVVLGSHLIDDYGNTYRmieqDDFDINTRLHTIvrGEDEAAMVESVGLALVKLPDVLNRLKPDIMIVHGDRFDA 116
Cdd:pfam02350   6 DPLELQLIVTGQHLSREMGDTFF----EGFGIPKPDYLL--NSDSQSLAKSTGLILIGLEDVLAEEKPDLVLVLGDTNET 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298566312  117 LALATSAALMNIRILHIEGGEVS-----GTIDDSIRHAITKLAHYHVCCTRSAEQHLISMCEDHDRILLAGCPSYDKLLs 191
Cdd:pfam02350  80 LAGALAAFYLRIPVAHVEAGLRSfdltePMPEEINRHAIDKLSDLHFAPTEEARENLLQEGEPPERIFVTGNTVIDALL- 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298566312  192 aknkDYMSIIRMWLG-DDVKSKDYIVALQHPVTT-DIKHSIKMFELTLDALISFNKRTLVL-FPNIDAGSKemvRVMRKk 268
Cdd:pfam02350 159 ----LSREEIEERSGiLAKLGKRYVLVTFHRRENeDDPEALRNILEALRALAERPDVPVVFpVHNNPRTRR---RLNER- 230

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298566312  269 gIEHHPNFRAVKHVPFDQFIQLVAHAGCMIGNSScGVR-EVGAFGTPVINL---GTRQIGRETGENVLhvrdADTQ-DKI 343
Cdd:pfam02350 231 -LEGYPRVRLIEPLGYLDFLSLLKRADLVITDSG-GIQeEAPSLGVPVVNLrdtTERPEGREAGTNVL----VGTDpERI 304

                         330       340       350
                  ....*....|....*....|....*....|..
gi 298566312  344 LQALHLQFGKQYPCSKIYGDGNAVPRILKFLK 375
Cdd:pfam02350 305 VAALERLLEDPASYKNPYGDGNASERIVDILE 336
NagC COG1940
Sugar kinase of the NBD/HSP70 family, may contain an N-terminal HTH domain [Carbohydrate ...
 481-641 1.13e-29

Sugar kinase of the NBD/HSP70 family, may contain an N-terminal HTH domain [Carbohydrate transport and metabolism, Transcription];


Pssm-ID: 441543 [Multi-domain]  Cd Length: 306  Bit Score: 119.23  E-value: 1.13e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298566312 481 ELIHGSSFCAAELGHLVVSLDGPDCSCGSHGCIEAYASGMALQREAKKLHdedlllvegmsvpKDEAVGALHLIQAAKLG 560
Cdd:COG1940  154 KLLRGANGNAGEIGHMPVDPDGPLCGCGNRGCLETYASGPALLRRARELG-------------GAEKLTAEELFAAARAG 220

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298566312 561 NAKAQSILRTAGTALGLGVVNILHTMNPSLVILSGVLAS---HYIHIVKDVIRQQALSSVQDVD--VVVSDLVDPALLGA 635
Cdd:COG1940  221 DPLALEVLDEAARYLGIGLANLINLLDPEVIVLGGGVSAagdLLLEPIREALAKYALPPAREDPriVPASLGDDAGLLGA 300


                 ....*.
gi 298566312 636 ASMVLD 641
Cdd:COG1940  301 AALALE 306
WecB COG0381
UDP-N-acetylglucosamine 2-epimerase [Cell wall/membrane/envelope biogenesis];
24-376 2.97e-19

UDP-N-acetylglucosamine 2-epimerase [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440150  Cd Length: 366  Bit Score: 89.74  E-value: 2.97e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298566312  24 KLAPIMFGIKTEPEFfELDVVVLGSHliddYgnTYRMIEQ--DDFDINT---RLHtiVRGEDEAAMVesvGLALVKLPDV 98
Cdd:COG0381   16 KMAPVIRALKKRPGF-EHVLVHTGQH----Y--DYEMSDQffEELGIPKpdyDLG--IGSGSLAEQT---ARILEGLEEV 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298566312  99 LNRLKPDIMIVHGD------------RfdalalatsaalMNIRILHIEGGEVSGTIDDS--I-RHAITKLAHYHVCCTRS 163
Cdd:COG0381   84 LEEEKPDAVLVHGDtnstlaaalaafK------------LGIPVAHVEAGLRSFDRPMPeeInRRLTDHISDLHFAPTEL 151

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298566312 164 AEQHLISMCEDHDRILLAGCPSYDKLLSAKNKDYMSIIRMWLGddVKSKDYIVALQH-PVTTDIKHSIKMFeltLDALIS 242
Cdd:COG0381  152 ARENLLREGIPPERIFVTGNTVIDALLYVLERAEESDILEELG--LEPKKYILVTLHrRENVDDPERLENI---LEALRE 226

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298566312 243 FNKRTL--VLFPnIDAGSKEMVrvmrKKGIEHHPNFRAVKHVPFDQFIQLVAHAGCMI---GnsscGV-REVGAFGTPVI 316
Cdd:COG0381  227 LAERYDlpVVFP-VHPRTRKRL----EEFLGGHPNIRLIEPLGYLDFLNLMKRAYLVLtdsG----GIqEEAPSLGKPCL 297

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 298566312 317 NL--GT-RQIGRETGENVLhVrDADTqDKILQALH--LQFGKQYPCSK----IYGDGNAVPRILKFLKS 376
Cdd:COG0381  298 TLrdTTeRPETVEAGTNKL-V-GTDP-ERIVAAVErlLDDPAAYERMAravnPYGDGNASERIVDILLR 363
ROK pfam00480
ROK family; This family, known as ROK (Repressor, ORF, Kinase) includes the xylose operon ...
 481-595 4.85e-15

ROK family; This family, known as ROK (Repressor, ORF, Kinase) includes the xylose operon repressor, xylR, from Bacillus subtilis, Lactobacillus pentosus and Staphylococcus xylosus; N-acetylglucosamine repressor, nagC, from Escherichia coli; glucokinase from Streptomyces coelicolor; fructokinase from from Pediococcus pentosaceus, Streptococcus mutans and Zymomonas mobilis; allokinase and mlc from E. coli; and E. coli hypothetical proteins yajF and yhcI and the corresponding Haemophilus influenzae proteins. The repressor proteins (xylR and nagC) from this family possess an N-terminal region not present in the sugar kinases and which contains an helix-turn-helix DNA-binding motif.


Pssm-ID: 395384 [Multi-domain]  Cd Length: 292  Bit Score: 76.22  E-value: 4.85e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298566312  481 ELIHGSSFCAAELGHLVVSLDGPDCSCGSHGCIEAYASGMALQREAKKlhdedlllvegmsvpKDEAVGALHLIQAAKLG 560
Cdd:pfam00480 142 KLFTGRNGVAGEIGHIQLDPNGPKCGCGNHGCLETIASGRALEKRYQQ---------------KGEDLEGKDIIVLAEQG 206

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 298566312  561 NAKAQSILRTAGTALGLGVVNILHTMNPSLVILSG 595
Cdd:pfam00480 207 DEVAEEAVERLARYLAKAIANLINLFDPQAIVLGG 241
ROK_glcA_fam TIGR00744
ROK family protein (putative glucokinase); This model models one branch of the ROK superfamily ...
 481-595 8.03e-14

ROK family protein (putative glucokinase); This model models one branch of the ROK superfamily of proteins. The three members of the seed alignment for this model all have experimental evidence for activity as glucokinase, but the set of related proteins is crowded with paralogs of different or unknown function. Proteins scoring above the trusted_cutoff will show strong similarity to at least one known glucokinase and may be designated as putative glucokinases. However, definitive identification of glucokinases should be done only with extreme caution. [Unknown function, General]


Pssm-ID: 273246 [Multi-domain]  Cd Length: 318  Bit Score: 73.01  E-value: 8.03e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298566312  481 ELIHGSSFCAAELGHLVVSLDGP-DCSCGSHGCIEAYASGMALQREAKKLHDEDLLLVEGMSVPKDEAVGALHLIQAAKL 559
Cdd:TIGR00744 144 EIRHGHNGVGAEIGHIRMVPDGRlLCNCGKQGCIETYASATGLVRYAKRANAKPERAEVLLALGDGDGISAKHVFVAARQ 223

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 298566312  560 GNAKAQSILRTAGTALGLGVVNILHTMNPSLVILSG 595
Cdd:TIGR00744 224 GDPVAVDSYREVARWAGAGLADLASLFNPSAIVLGG 259
PRK05082 PRK05082
N-acetylmannosamine kinase; Provisional
 479-612 3.44e-08

N-acetylmannosamine kinase; Provisional


Pssm-ID: 235338 [Multi-domain]  Cd Length: 291  Bit Score: 55.30  E-value: 3.44e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298566312 479 QHELIHGSSFCAAELGHLVVSLDGPDCSCGSHGCIEAYASGMALQREAKKLhdedlllvegmsvpKDEAVGALHLIQAAK 558
Cdd:PRK05082 140 NGKLLTGPGGLAGHIGHTLADPHGPVCGCGRRGCVEAIASGRAIAAAAQGW--------------LAGCDAKTIFERAGQ 205

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 298566312 559 lGNAKAQSILRTAGTALGLGVVNILHTMNPSLVILSGV--LASHYIHIVKDVIRQQ 612
Cdd:PRK05082 206 -GDEQAQALINRSAQAIARLIADLKATLDCQCVVLGGSvgLAEGYLELVQAYLAQE 260
 
Name Accession Description Interval E-value
NeuC_NnaA TIGR03568
UDP-N-acetyl-D-glucosamine 2-epimerase, UDP-hydrolysing; This family of enzymes catalyzes the ...
 11-374 3.21e-129

UDP-N-acetyl-D-glucosamine 2-epimerase, UDP-hydrolysing; This family of enzymes catalyzes the combined epimerization and UDP-hydrolysis of UDP-N-acetylglucosamine to N-acetylmannosamine. This is in contrast to the related enzyme WecB (TIGR00236) which retains the UDP moiety. NeuC acts in concert with NeuA and NeuB to synthesize CMP-N5-acetyl-neuraminate.


Pssm-ID: 274654  Cd Length: 364  Bit Score: 384.96  E-value: 3.21e-129
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298566312   11 RVCVATCNRADYSKLAPIMFGIKTEPEFfELDVVVLGSHLIDDYGNTYRMIEQDDFDINTRLHTIVRGEDEAAMVESVGL 90
Cdd:TIGR03568   1 KICVVTGTRADYGLLRPLLKALQDDPDL-ELQLIVTGMHLSPEYGNTVNEIEKDGFDIDEKIEILLDSDSNAGMAKSMGL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298566312   91 ALVKLPDVLNRLKPDIMIVHGDRFDALALATSAALMNIRILHIEGGEVS-GTIDDSIRHAITKLAHYHVCCTRSAEQHLI 169
Cdd:TIGR03568  80 TIIGFSDAFERLKPDLVVVLGDRFEMLAAAIAAALLNIPIAHIHGGEVTeGAIDESIRHAITKLSHLHFVATEEYRQRVI 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298566312  170 SMCEDHDRILLAGCPSYDKLlsaKNKDYMS--IIRMWLGDDvKSKDYIVALQHPVTTDIKHSIKMFELTLDALISFNKRT 247
Cdd:TIGR03568 160 QMGEDPDRVFNVGSPGLDNI---LSLDLLSkeELEEKLGID-LDKPYALVTFHPVTLEKAEAEEQIKELLKALDELNKNI 235

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298566312  248 LVLFPNIDAGSKEMVRVMRKKgIEHHPNFRAVKHVPFDQFIQLVAHAGCMIGNSSCGVREVGAFGTPVINLGTRQIGRET 327
Cdd:TIGR03568 236 IFTYPNADAGSRIINEAIEEY-VEKHPNFRLFKSLGQERYLSLLKNADAVIGNSSSGIIEAPSFGVPTINIGTRQKGRLR 314

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|..
gi 298566312  328 GENVLHVrDADTQDkILQALHLQFGKQYPCSK-----IYGDGNAVPRILKFL 374
Cdd:TIGR03568 315 ADSVIDV-DPDKEE-IVKAIEKALDPAFKKSLkkvknPYGDGNSSKRIIEIL 364
ASKHA_NBD_ROK_GNE cd24060
nucleotide-binding domain (NBD) of bifunctional UDP-N-acetylglucosamine 2-epimerase ...
 408-638 7.78e-126

nucleotide-binding domain (NBD) of bifunctional UDP-N-acetylglucosamine 2-epimerase/N-acetylmannosamine kinase (GNE) and similar proteins; GNE (EC 3.2.1.183/EC 2.7.1.60), also called UDP-GlcNAc-2-epimerase/ManAc kinase, is a bi-functional enzyme that plays a key role in sialic acid biosynthesis. It regulates and initiates biosynthesis of N-acetylneuraminic acid (NeuAc), a precursor of sialic acids. It plays an essential role in early development and required for normal sialylation in hematopoietic cells. Sialylation is implicated in cell adhesion, signal transduction, tumorigenicity and metastatic behavior of malignant cells. GNE is the only human protein that contains a kinase domain belonging to the ROK (repressor, ORF, kinase) family. Mutations of the GNE protein cause sialurea or autosomal recessive inclusion body myopathy/Nonaka myopathy.


Pssm-ID: 466910 [Multi-domain]  Cd Length: 305  Bit Score: 374.06  E-value: 7.78e-126
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298566312 408 SALAVDLGGTNLRVAIVSMKGEIVKKYTQFNPKTYEERINLILQMCVEAAAEAVKLNCRILGVGIGGG------------ 475
Cdd:cd24060    1 SALAVDLGGTNLRVAIVSMKGEIVKKYTQPNPKTYEERIDLILQMCVEAASEAVKLNCRILGVGISTGgrvnpregivlh 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298566312 476 --------------------------------------------------------------IIHQHELIHGSSFCAAEL 493
Cdd:cd24060   81 stkliqewssvdlrtpisdalhlpvwvdndgncaalaerkfghgkgvenfvtvitgtgigggIILNHELIHGSSFCAAEL 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298566312 494 GHLVVSLDGPDCSCGSHGCIEAYASGMALQREAKKLHDEDLLLVEGMSVPKDEAVGALHLIQAAKLGNAKAQSILRTAGT 573
Cdd:cd24060  161 GHIVVSLDGPDCMCGSHGCVEAYASGMALQREAKKLHDEDLLLVEGMSVTNDEEVTAKHLIQAAKLGNAKAQKILRTAGT 240

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 298566312 574 ALGLGVVNILHTMNPSLVILSGVLASHYIHIVKDVIRQQALSSVQDVDVVVSDLVDPALLGAASM 638
Cdd:cd24060  241 ALGLGIVNILHTLNPSLVILSGVLASHYENIVKDVIAQRALPSVQNVDVVVSDLVDPALLGAASM 305
GTB_UDP-GlcNAc_2-Epimerase cd03786
UDP-N-acetylglucosamine 2-epimerase and similar proteins; Bacterial members of the ...
 11-375 2.81e-103

UDP-N-acetylglucosamine 2-epimerase and similar proteins; Bacterial members of the UDP-N-Acetylglucosamine (GlcNAc) 2-Epimerase family (EC 5.1.3.14) are known to catalyze the reversible interconversion of UDP-GlcNAc and UDP-N-acetylmannosamine (UDP-ManNAc). The enzyme serves to produce an activated form of ManNAc residues (UDP-ManNAc) for use in the biosynthesis of a variety of cell surface polysaccharides; The mammalian enzyme is bifunctional, catalyzing both the inversion of stereochemistry at C-2 and the hydrolysis of the UDP-sugar linkage to generate free ManNAc. It also catalyzes the phosphorylation of ManNAc to generate ManNAc 6-phosphate, a precursor to salic acids. In mammals, sialic acids are found at the termini of oligosaccharides in a large variety of cell surface glycoconjugates and are key mediators of cell-cell recognition events. Mutations in human members of this family have been associated with Sialuria, a rare disease caused by the disorders of sialic acid metabolism. This family belongs to the GT-B structural superfamily of glycoslytransferases, which have characteristic N- and C-terminal domains each containing a typical Rossmann fold. The two domains have high structural homology despite minimal sequence homology. The large cleft that separates the two domains includes the catalytic center and permits a high degree of flexibility.


Pssm-ID: 340819 [Multi-domain]  Cd Length: 365  Bit Score: 318.38  E-value: 2.81e-103
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298566312  11 RVCVATCNRADYSKLAPIMFGIKTEPEFfELDVVVLGSHLIDDYGNTYRMIEqddFDINTRLHTIVRGEDEAAMVESVGL 90
Cdd:cd03786    1 KILTVTGTRPEAIKLAPVLRALKKDPGL-ELVLVVTGQHLDMLLGVLFFFIL---FLIKPDYDLDLMGDNQTLGAKTGGL 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298566312  91 aLVKLPDVLNRLKPDIMIVHGDRFDALALATSAALMNIRILHIEGGEVS---GTIDDSIRHAITKLAHYHVCCTRSAEQH 167
Cdd:cd03786   77 -LIGLEEVLFEEKPDAVLVLGDTNTTLAGALAAFKLGIPVAHVEAGLRSfdlGMPEEENRHRIDKLSDLHFAPTEEAREN 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298566312 168 LISMCEDHDRILLAGCPSYDKLLSAKNKDYMSIIrmWLGDDVKSKDYIVALQHPVTTDikHSIKMFELTLDALISFNKR- 246
Cdd:cd03786  156 LLQEGEPPERIFVTGNTVIDALLSAALRIRDELV--LSKLGLLEKKYILVTLHRRENV--DSGERLEELLEALEELAEKy 231

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298566312 247 -TLVLFPNIDAGSKEMVRVMRKKgIEHHPNFRAVKHVPFDQFIQLVAHAGCMIGNSScGVREVGAF-GTPVINLGTRQIG 324
Cdd:cd03786  232 dLIVVYPNHPRTRPRIREVGLKF-LGGLPNIRLIDPLGYLDLVLLKKRAKLVLTDSG-GIQEEASFlGKPVLVLRDRTER 309

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 298566312 325 RETGENVLHVRDADTQDKILQALHLQFGKQYPCSK-----IYGDGNAVPRILKFLK 375
Cdd:cd03786  310 PERVEAGTNVLVGTDPEAILEAIEKLLSDEFEYSRmsainPYGDGNASERIVDILE 365
Epimerase_2 pfam02350
UDP-N-acetylglucosamine 2-epimerase; This family consists of UDP-N-acetylglucosamine ...
 37-375 2.77e-61

UDP-N-acetylglucosamine 2-epimerase; This family consists of UDP-N-acetylglucosamine 2-epimerases EC:5.1.3.14 this enzyme catalyzes the production of UDP-ManNAc from UDP-GlcNAc. Note that some of the enzymes is this family are bifunctional such as Swiss:O35826 and Swiss:Q9Z0P6 in this instance Pfam matches only the N-terminal half of the protein suggesting that the additional C-terminal part (when compared to mono-functional members of this family) is responsible for the UPD-N-acetylmannosamine kinase activity of these enzymes. This hypothesis is further supported by the assumption that the C-terminal part of Swiss:O35826 is the kinase domain.


Pssm-ID: 426733 [Multi-domain]  Cd Length: 336  Bit Score: 207.39  E-value: 2.77e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298566312   37 EFFELDVVVLGSHLIDDYGNTYRmieqDDFDINTRLHTIvrGEDEAAMVESVGLALVKLPDVLNRLKPDIMIVHGDRFDA 116
Cdd:pfam02350   6 DPLELQLIVTGQHLSREMGDTFF----EGFGIPKPDYLL--NSDSQSLAKSTGLILIGLEDVLAEEKPDLVLVLGDTNET 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298566312  117 LALATSAALMNIRILHIEGGEVS-----GTIDDSIRHAITKLAHYHVCCTRSAEQHLISMCEDHDRILLAGCPSYDKLLs 191
Cdd:pfam02350  80 LAGALAAFYLRIPVAHVEAGLRSfdltePMPEEINRHAIDKLSDLHFAPTEEARENLLQEGEPPERIFVTGNTVIDALL- 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298566312  192 aknkDYMSIIRMWLG-DDVKSKDYIVALQHPVTT-DIKHSIKMFELTLDALISFNKRTLVL-FPNIDAGSKemvRVMRKk 268
Cdd:pfam02350 159 ----LSREEIEERSGiLAKLGKRYVLVTFHRRENeDDPEALRNILEALRALAERPDVPVVFpVHNNPRTRR---RLNER- 230

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298566312  269 gIEHHPNFRAVKHVPFDQFIQLVAHAGCMIGNSScGVR-EVGAFGTPVINL---GTRQIGRETGENVLhvrdADTQ-DKI 343
Cdd:pfam02350 231 -LEGYPRVRLIEPLGYLDFLSLLKRADLVITDSG-GIQeEAPSLGVPVVNLrdtTERPEGREAGTNVL----VGTDpERI 304

                         330       340       350
                  ....*....|....*....|....*....|..
gi 298566312  344 LQALHLQFGKQYPCSKIYGDGNAVPRILKFLK 375
Cdd:pfam02350 305 VAALERLLEDPASYKNPYGDGNASERIVDILE 336
NagC COG1940
Sugar kinase of the NBD/HSP70 family, may contain an N-terminal HTH domain [Carbohydrate ...
 481-641 1.13e-29

Sugar kinase of the NBD/HSP70 family, may contain an N-terminal HTH domain [Carbohydrate transport and metabolism, Transcription];


Pssm-ID: 441543 [Multi-domain]  Cd Length: 306  Bit Score: 119.23  E-value: 1.13e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298566312 481 ELIHGSSFCAAELGHLVVSLDGPDCSCGSHGCIEAYASGMALQREAKKLHdedlllvegmsvpKDEAVGALHLIQAAKLG 560
Cdd:COG1940  154 KLLRGANGNAGEIGHMPVDPDGPLCGCGNRGCLETYASGPALLRRARELG-------------GAEKLTAEELFAAARAG 220

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298566312 561 NAKAQSILRTAGTALGLGVVNILHTMNPSLVILSGVLAS---HYIHIVKDVIRQQALSSVQDVD--VVVSDLVDPALLGA 635
Cdd:COG1940  221 DPLALEVLDEAARYLGIGLANLINLLDPEVIVLGGGVSAagdLLLEPIREALAKYALPPAREDPriVPASLGDDAGLLGA 300


                 ....*.
gi 298566312 636 ASMVLD 641
Cdd:COG1940  301 AALALE 306
ASKHA_ATPase_ROK_BsXylR-like cd24076
ATPase-like domain of Bacillus subtilis xylose repressor (XylR) and similar proteins; This ...
 481-641 1.43e-29

ATPase-like domain of Bacillus subtilis xylose repressor (XylR) and similar proteins; This subfamily includes a group of uncharacterized proteins similar to Bacillus subtilis xylose repressor (BsXylR), which belongs to the kinase (ROK) family, a group of proteins that have sugar kinase and/or transcriptional repressor activities. BsXylR acts as transcriptional repressor of xylose-utilizing enzymes.


Pssm-ID: 466926 [Multi-domain]  Cd Length: 303  Bit Score: 118.82  E-value: 1.43e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298566312 481 ELIHGSSFCAAELGHLVVSLDGPDCSCGSHGCIEAYASGMALQREAKKLHDEdlllVEGMSVPKdeavgalhLIQAAKLG 560
Cdd:cd24076  149 ELYRGASGFAGEIGHMTVDPDGPPCSCGNRGCWETYASERALLRAAGRLGAG----GEPLSLAE--------LVEAARAG 216

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298566312 561 NAKAQSILRTAGTALGLGVVNILHTMNPSLVILSGVLAS---HYIHIVKDVIRQQALSSVQDVDVVVSDL--VDPALLGA 635
Cdd:cd24076  217 DPAALAALEEVGEYLGIGLANLVNTFNPELVVLGGALAPlgpWLLPPLRAEVARRALPAPARDVRIVVSRlgEDAAALGA 296


                 ....*.
gi 298566312 636 ASMVLD 641
Cdd:cd24076  297 AALAID 302
ASKHA_ATPase_ROK_CYANR cd24073
ATPase-like domain of cyclobis-(1-6)-alpha-nigerosyl repressor (CYANR) and similar proteins; ...
 478-595 2.01e-27

ATPase-like domain of cyclobis-(1-6)-alpha-nigerosyl repressor (CYANR) and similar proteins; CYANR acts as transcriptional repressor of cyclobis-(1-6)-alpha-nigerosyl (CNN) degrading enzymes. Members of this subfamily belong to the kinase (ROK) family, a group of proteins that have sugar kinase and/or transcriptional repressor activities.


Pssm-ID: 466923 [Multi-domain]  Cd Length: 304  Bit Score: 112.65  E-value: 2.01e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298566312 478 HQHELIHGSSFCAAELGHLVVSLDGPDCSCGSHGCIEAYASGMALQREAKKLHdedlllvegmsvPKDEAVGALHLIQAA 557
Cdd:cd24073  145 VDGRLYRGAHGGAGEIGHTTVDPDGPPCRCGKRGCLEAYASDPAILRQAREAG------------LRGEPLTIEDLLAAA 212

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 298566312 558 KLGNAKAQSILRTAGTALGLGVVNILHTMNPSLVILSG 595
Cdd:cd24073  213 RAGDPAARAILRRAGRALGLALANLVNLLDPELIIISG 250
ASKHA_NBD_ROK_TM1224-like cd24059
nucleotide-binding domain (NBD) of Thermotoga maritima N-acetylglucosamine kinase (TM1224) and ...
 479-642 6.42e-23

nucleotide-binding domain (NBD) of Thermotoga maritima N-acetylglucosamine kinase (TM1224) and similar proteins; This subfamily includes a group of uncharacterized proteins similar to N-acetylglucosamine kinase (Tm1224; EC 2.7.1.59) from Thermotoga maritima, which belongs to kinase (ROK) family, a group of proteins that have sugar kinase and/or transcriptional repressor activities. Tm1224 lacks the cysteine-rich zinc-binding motif, which presents in other family members.


Pssm-ID: 466909 [Multi-domain]  Cd Length: 305  Bit Score: 99.58  E-value: 6.42e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298566312 479 QHELIHGSSFCAAELGHLVVSLDGPDCSCGSHGCIEAYASGMALQREAKKlhdedlllvEGMSVPKDEavgaLHLIQAAK 558
Cdd:cd24059  147 NGKLYRGVDGYAGEIGHTSIDINGPRCSCGNRGCLELYASIPAIEKKARS---------ALGSGRSFQ----LDIVEALQ 213

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298566312 559 LGNAKAQSILRTAGTALGLGVVNILHTMNPSLVILSGVLA---SHYIHIVKDVIRQQALSSVQDVDVVVSDL--VDPALL 633
Cdd:cd24059  214 KGDPIADEVIEEAAKYLGIGLVNLINLLNPEAIIIGGELIylgERYLEPIEKEVNSRLFGRNAREVRILKSSlgEDAPLL 293


                 ....*....
gi 298566312 634 GAASMVLDY 642
Cdd:cd24059  294 GAAALVLNK 302
ASKHA_NBD_ROK_FnNanK-like cd24068
nucleotide-binding domain (NBD) of Fusobacterium nucleatum N-acetylmannosamine kinase and ...
 479-595 2.55e-21

nucleotide-binding domain (NBD) of Fusobacterium nucleatum N-acetylmannosamine kinase and similar proteins; The family includes Fusobacterium nucleatum N-acetylmannosamine kinase (NanK; EC 2.7.1.60) and beta-glucoside kinase (BglK; EC 2.7.1.85) from Klebsiella pneumoniae and Listeria innocua. NanK catalyzes the second step of the sialic acid catabolic pathway, transferring a phosphate group from adenosine 5'-triphosphate to the C6 position of N-acetylmannosamine to generate N-acetylmannosamine 6-phosphate. Unlike other NanK enzymes and ROK family members, F. nucleatum NanK does not have a conserved zinc-binding site. BglK catalyzes the ATP-dependent phosphorylation of cellobiose to produce cellobiose-6'-P. It may have a dual role of kinase and transcriptional regulator of the cellobiose-PTS operon. The subfamily belongs to the kinase (ROK) family, a group of proteins that have sugar kinase and/or transcriptional repressor activities. Members of this subfamily lack the cysteine-rich zinc-binding motif, which presents in other ROK families.


Pssm-ID: 466918 [Multi-domain]  Cd Length: 294  Bit Score: 94.55  E-value: 2.55e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298566312 479 QHELIHGSSFCAAELGHLVVSLDGPDCSCGSHGCIEAYASGMALQREAKKLHDEDLLlvegmsvpkdeavGALHLIQAAK 558
Cdd:cd24068  143 DGRLYRGANGSAGELGHMVVDPGGRPCCCGGKGCLEQYASGTALVRRVAEALGEPGI-------------DGREIFDLAD 209

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 298566312 559 LGNAKAQSILRTAGTALGLGVVNILHTMNPSLVILSG 595
Cdd:cd24068  210 AGDPLAKEVVEEFAEDLATGLANLVHIFDPEVIVIGG 246
ASKHA_ATPase_ROK_YphH-like cd24072
ATPase-like domain of Escherichia coli protein YphH and similar proteins; This subfamily ...
 481-611 1.17e-19

ATPase-like domain of Escherichia coli protein YphH and similar proteins; This subfamily includes a group of uncharacterized proteins similar to Escherichia coli protein YphH that belongs to the kinase (ROK) family, a group of proteins that have sugar kinase and/or transcriptional repressor activities.


Pssm-ID: 466922 [Multi-domain]  Cd Length: 308  Bit Score: 90.17  E-value: 1.17e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298566312 481 ELIHGSSFCAAELGHLVVSLDGPDCSCGSHGCIEAYASGMALQREAKKlhdedlLLVEGMSVPKDEAVGALHLIQAAKLG 560
Cdd:cd24072  146 KLYIGASSGSGEIGHTKVNPDGARCDCGRRGCLETVASNSALKRNARV------TLKLGPVSADPEKLTMEQLIEALEEG 219

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 298566312 561 NAKAQSILRTAGTALGLGVVNILHTMNPSLVILSGVLASHYIHIVKDVIRQ 611
Cdd:cd24072  220 EPIATQIFDRAANAIGRSLANILNLLNPEQVLLYGRGCRAGDLLLPAIRRA 270
WecB COG0381
UDP-N-acetylglucosamine 2-epimerase [Cell wall/membrane/envelope biogenesis];
24-376 2.97e-19

UDP-N-acetylglucosamine 2-epimerase [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440150  Cd Length: 366  Bit Score: 89.74  E-value: 2.97e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298566312  24 KLAPIMFGIKTEPEFfELDVVVLGSHliddYgnTYRMIEQ--DDFDINT---RLHtiVRGEDEAAMVesvGLALVKLPDV 98
Cdd:COG0381   16 KMAPVIRALKKRPGF-EHVLVHTGQH----Y--DYEMSDQffEELGIPKpdyDLG--IGSGSLAEQT---ARILEGLEEV 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298566312  99 LNRLKPDIMIVHGD------------RfdalalatsaalMNIRILHIEGGEVSGTIDDS--I-RHAITKLAHYHVCCTRS 163
Cdd:COG0381   84 LEEEKPDAVLVHGDtnstlaaalaafK------------LGIPVAHVEAGLRSFDRPMPeeInRRLTDHISDLHFAPTEL 151

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298566312 164 AEQHLISMCEDHDRILLAGCPSYDKLLSAKNKDYMSIIRMWLGddVKSKDYIVALQH-PVTTDIKHSIKMFeltLDALIS 242
Cdd:COG0381  152 ARENLLREGIPPERIFVTGNTVIDALLYVLERAEESDILEELG--LEPKKYILVTLHrRENVDDPERLENI---LEALRE 226

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298566312 243 FNKRTL--VLFPnIDAGSKEMVrvmrKKGIEHHPNFRAVKHVPFDQFIQLVAHAGCMI---GnsscGV-REVGAFGTPVI 316
Cdd:COG0381  227 LAERYDlpVVFP-VHPRTRKRL----EEFLGGHPNIRLIEPLGYLDFLNLMKRAYLVLtdsG----GIqEEAPSLGKPCL 297

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 298566312 317 NL--GT-RQIGRETGENVLhVrDADTqDKILQALH--LQFGKQYPCSK----IYGDGNAVPRILKFLKS 376
Cdd:COG0381  298 TLrdTTeRPETVEAGTNKL-V-GTDP-ERIVAAVErlLDDPAAYERMAravnPYGDGNASERIVDILLR 363
ASKHA_ATPase_ROK_Lmo0178-like cd24071
ATPase-like domain of Listeria monocytogenes Lmo0178 and similar proteins; This subfamily ...
 482-595 4.41e-19

ATPase-like domain of Listeria monocytogenes Lmo0178 and similar proteins; This subfamily includes a group of uncharacterized proteins similar to Listeria monocytogenes Lmo0178 protein, which is a predicted transcription repressor belonging to the kinase (ROK) family, a group of proteins that have sugar kinase and/or transcriptional repressor activities.


Pssm-ID: 466921 [Multi-domain]  Cd Length: 312  Bit Score: 88.50  E-value: 4.41e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298566312 482 LIHGSSFCAAELGHLVVSLDGPDCSCGSHGCIEAYASGMALQREAKKLHDEDLLLvegmSVPKDEAVGALHLIQAAKLGN 561
Cdd:cd24071  149 LYTGNFGGAGEIGHMTIQPDGRKCYCGQKGCLEAYASFEALVNEIKELTESYPLS----LLKELEDFEIEKVREAAEEGD 224

                         90       100       110
                 ....*....|....*....|....*....|....
gi 298566312 562 AKAQSILRTAGTALGLGVVNILHTMNPSLVILSG 595
Cdd:cd24071  225 SVATELFKKAGEYLGIGIKNLINIFNPEAIIIGG 258
ASKHA_NBD_ROK_SgGLK-like cd24061
nucleotide-binding domain (NBD) of Streptomyces griseus glucokinase (GLK) and similar proteins; ...
 481-598 1.22e-18

nucleotide-binding domain (NBD) of Streptomyces griseus glucokinase (GLK) and similar proteins; Glucokinase (EC 2.7.1.2), also called glucose kinase, acts as an ATP-dependent kinase that phosphorylates glucose using ATP as a donor to give glucose-6-phosphate and ADP. It is highly specific for glucose. Glucokinases are found in invertebrates and microorganisms. They belong to the kinase (ROK) family, a group of proteins that have sugar kinase and/or transcriptional repressor activities.


Pssm-ID: 466911 [Multi-domain]  Cd Length: 306  Bit Score: 87.02  E-value: 1.22e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298566312 481 ELIHGSSFCAAELGHLVVSLDGPDCSCGSHGCIEAYASGMALQREAKKLHDED-----LLLVEGmsvpKDEAVGALHLIQ 555
Cdd:cd24061  140 KLLRGAFGIAGEFGHIRVVPDGLLCGCGSRGCWEQYASGRALVRYAKEAANATpegaaVLLADG----SVDGITGKHISE 215

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 298566312 556 AAKLGNAKAQSILRTAGTALGLGVVNILHTMNPSLVILSGVLA 598
Cdd:cd24061  216 AARAGDPVALDALRELARWLGAGLASLAALLDPELFVIGGGVS 258
ASKHA_NBD_ROK_TmGLK-like cd24064
nucleotide-binding domain (NBD) of Thermotoga maritima glucokinase (GLK) and similar proteins; ...
 482-595 4.41e-18

nucleotide-binding domain (NBD) of Thermotoga maritima glucokinase (GLK) and similar proteins; Glucokinase (EC 2.7.1.2), also called glucose kinase, acts as an ATP-dependent kinase that phosphorylates glucose using ATP as a donor to give glucose-6-phosphate and ADP. It is highly specific for glucose. Glucokinases are found in invertebrates and microorganisms. They belong to the kinase (ROK) family, a group of proteins that have sugar kinase and/or transcriptional repressor activities.


Pssm-ID: 466914 [Multi-domain]  Cd Length: 301  Bit Score: 85.24  E-value: 4.41e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298566312 482 LIHGSSFCAAELGHLVVSLDGPDCSCGSHGCIEAYASGMALQREAKKLHDE--DLLlvegmsVPKDEAVGALHLIQAAKL 559
Cdd:cd24064  144 LLTGYDGIAAELGHVIVEPNGPICGCGNRGCVEAFASATAIIRYARESRKRypDSL------AGESEKINAKHVFDAARK 217

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 298566312 560 GNAKAQSILRTAGTALGLGVVNILHTMNPSLVILSG 595
Cdd:cd24064  218 NDPLATMVFRRVVDALAIAIGGFVHIFNPEIIIIGG 253
ASKHA_NBD_ROK_ApGLK-like cd24063
nucleotide-binding domain (NBD) of Aeropyrum pernix glucokinase (GLK) and similar proteins; ...
 482-611 2.06e-17

nucleotide-binding domain (NBD) of Aeropyrum pernix glucokinase (GLK) and similar proteins; Glucokinase (EC 2.7.1.2), also called glucose kinase, acts as an ATP-dependent kinase that phosphorylates glucose using ATP as a donor to give glucose-6-phosphate and ADP. It is highly specific for glucose. Glucokinases are found in invertebrates and microorganisms. They belong to the kinase (ROK) family, a group of proteins that have sugar kinase and/or transcriptional repressor activities.


Pssm-ID: 466913 [Multi-domain]  Cd Length: 308  Bit Score: 83.54  E-value: 2.06e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298566312 482 LIHGSSFCAAELGHLVVSLD-GPDCSCGSHGCIEAYASGMALQREAKKL-HDEDLLLVEGMSVPKDEAVGALHLIQAAKL 559
Cdd:cd24063  147 LLLGKNGNAAEVGHLVVDTEsGLKCGCGGYGHWEAFASGRGIPRFAREWaEGFSSRTSLKLRNPGGEGITAKEVFSAARK 226

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 298566312 560 GNAKAQSILRTAGTALGLGVVNILHTMNPSLVILSGVLASHYIHIVKDVIRQ 611
Cdd:cd24063  227 GDPLALKIIEKLARYNGRGIANVINAYDPELIVIGGSVFNNNKDILDPLIEY 278
ASKHA_NBD_ROK_TtHK-like cd24065
nucleotide-binding domain (NBD) of Thermus thermophilus hexokinase (HK) and similar proteins; ...
 481-612 1.31e-16

nucleotide-binding domain (NBD) of Thermus thermophilus hexokinase (HK) and similar proteins; HK (EC 2.7.1.1) possesses the ability to transfer an inorganic phosphate group from ATP to a substrate. It catalyzes the ATP-dependent phosphorylation of aldo- and keto-hexose sugars to the hexose-6-phosphate (H6P). Thermus thermophilus HK possesses significant enzymatic activity against glucose and mannose. However, it shows little catalytic capacity for galactose and fructose. Members of this subfamily belong to the kinase (ROK) family, a group of proteins that have sugar kinase and/or transcriptional repressor activities.


Pssm-ID: 466915 [Multi-domain]  Cd Length: 289  Bit Score: 80.84  E-value: 1.31e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298566312 481 ELIHGSSFCAAELGHLVVSLDGPDCSCGSHGCIEAYASGMALQREAKKLHDEDlllvegMSVPKdeavgalhLIQAAKLG 560
Cdd:cd24065  143 RVLRGRHGQAGEIGHTTVLPGGPMCGCGLVGCLEALASGRALARDASFAYGRP------MSTAE--------LFELAQQG 208

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 298566312 561 NAKAQSILRTAGTALGLGVVNILHTMNPSLVILSGVLASH---YIHIVKDVIRQQ 612
Cdd:cd24065  209 EPKALRIVEQAAAHLGIGLANLQKALDPEVFVLGGGVAQVgdyYLLPVQEAARRY 263
ROK pfam00480
ROK family; This family, known as ROK (Repressor, ORF, Kinase) includes the xylose operon ...
 481-595 4.85e-15

ROK family; This family, known as ROK (Repressor, ORF, Kinase) includes the xylose operon repressor, xylR, from Bacillus subtilis, Lactobacillus pentosus and Staphylococcus xylosus; N-acetylglucosamine repressor, nagC, from Escherichia coli; glucokinase from Streptomyces coelicolor; fructokinase from from Pediococcus pentosaceus, Streptococcus mutans and Zymomonas mobilis; allokinase and mlc from E. coli; and E. coli hypothetical proteins yajF and yhcI and the corresponding Haemophilus influenzae proteins. The repressor proteins (xylR and nagC) from this family possess an N-terminal region not present in the sugar kinases and which contains an helix-turn-helix DNA-binding motif.


Pssm-ID: 395384 [Multi-domain]  Cd Length: 292  Bit Score: 76.22  E-value: 4.85e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298566312  481 ELIHGSSFCAAELGHLVVSLDGPDCSCGSHGCIEAYASGMALQREAKKlhdedlllvegmsvpKDEAVGALHLIQAAKLG 560
Cdd:pfam00480 142 KLFTGRNGVAGEIGHIQLDPNGPKCGCGNHGCLETIASGRALEKRYQQ---------------KGEDLEGKDIIVLAEQG 206

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 298566312  561 NAKAQSILRTAGTALGLGVVNILHTMNPSLVILSG 595
Cdd:pfam00480 207 DEVAEEAVERLARYLAKAIANLINLFDPQAIVLGG 241
wecB TIGR00236
UDP-N-acetylglucosamine 2-epimerase; This cytosolic enzyme converts UDP-N-acetyl-D-glucosamine ...
 10-375 5.63e-14

UDP-N-acetylglucosamine 2-epimerase; This cytosolic enzyme converts UDP-N-acetyl-D-glucosamine to UDP-N-acetyl-D-mannosamine. In E. coli, this is the first step in the pathway of enterobacterial common antigen biosynthesis.Members of this orthology group have many gene symbols, often reflecting the overall activity of the pathway and/or operon that includes it. Symbols include epsC (exopolysaccharide C) in Burkholderia solanacerum, cap8P (type 8 capsule P) in Staphylococcus aureus, and nfrC in an older designation based on the effects of deletion on phage N4 adsorption. Epimerase activity was also demonstrated in a bifunctional rat enzyme, for which the N-terminal domain appears to be orthologous. The set of proteins found above the suggested cutoff includes E. coli WecB in one of two deeply branched clusters and the rat UDP-N-acetylglucosamine 2-epimerase domain in the other. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides]


Pssm-ID: 272978  Cd Length: 365  Bit Score: 74.03  E-value: 5.63e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298566312   10 LRVCVATCNRADYSKLAPIMFGIKTEPeFFELDVVVLGSHliddygntYRMIEQ--DDFDINTRlHTIVRGEDEAAMVES 87
Cdd:TIGR00236   1 LKVMIVLGTRPEAIKMAPLIRALKKYP-EIDSYVIVTAQH--------REMLDQvlDLFHLPPD-YDLNIMSPGQTLGEI 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298566312   88 VGLALVKLPDVLNRLKPDIMIVHGDRFDALALATSAALMNIRILHIEGGEVSGTIDDSI-----RHAITKLAHYHVCCTR 162
Cdd:TIGR00236  71 TSNMLEGLEELLLEEKPDIVLVQGDTTTTLAGALAAFYLQIPVGHVEAGLRTGDRYSPMpeeinRQLTGHIADLHFAPTE 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298566312  163 SAEQHLISMCEDHDRILLAGCPSYDKLLSAKNKDYMSIIRMWLGDDvksKDYIVALQHPVTT------DIKHSIKmfelt 236
Cdd:TIGR00236 151 QAKDNLLRENVKADSIFVTGNTVIDALLTNVEIAYSSPVLSEFGED---KRMILLTLHRRENvgepleNIFKAIR----- 222

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298566312  237 ldALISFNKRTLVLFPnidAGSKEMVRVMRKKGIEHHPNFRAVKHVPFDQFIQLVAHAGCMIGNSSCGVREVGAFGTPVI 316
Cdd:TIGR00236 223 --EIVEEFEDVQIVYP---VHLNPVVREPLHKHLGDSKRVHLIEPLEYLDFLNLAANSHLILTDSGGVQEEAPSLGKPVL 297

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 298566312  317 NL---GTRQIGRETGENVLHvrdADTQDKILQALHLQFGKQYPCSKI------YGDGNAVPRILKFLK 375
Cdd:TIGR00236 298 VLrdtTERPETVEAGTNKLV---GTDKENITKAAKRLLTDPDEYKKMsnasnpYGDGEASERIVEELL 362
ROK_glcA_fam TIGR00744
ROK family protein (putative glucokinase); This model models one branch of the ROK superfamily ...
 481-595 8.03e-14

ROK family protein (putative glucokinase); This model models one branch of the ROK superfamily of proteins. The three members of the seed alignment for this model all have experimental evidence for activity as glucokinase, but the set of related proteins is crowded with paralogs of different or unknown function. Proteins scoring above the trusted_cutoff will show strong similarity to at least one known glucokinase and may be designated as putative glucokinases. However, definitive identification of glucokinases should be done only with extreme caution. [Unknown function, General]


Pssm-ID: 273246 [Multi-domain]  Cd Length: 318  Bit Score: 73.01  E-value: 8.03e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298566312  481 ELIHGSSFCAAELGHLVVSLDGP-DCSCGSHGCIEAYASGMALQREAKKLHDEDLLLVEGMSVPKDEAVGALHLIQAAKL 559
Cdd:TIGR00744 144 EIRHGHNGVGAEIGHIRMVPDGRlLCNCGKQGCIETYASATGLVRYAKRANAKPERAEVLLALGDGDGISAKHVFVAARQ 223

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 298566312  560 GNAKAQSILRTAGTALGLGVVNILHTMNPSLVILSG 595
Cdd:TIGR00744 224 GDPVAVDSYREVARWAGAGLADLASLFNPSAIVLGG 259
ASKHA_NBD_ROK_BsGLK-like cd24062
nucleotide-binding domain (NBD) of Bacillus subtilis glucokinase (GLK) and similar proteins; ...
 474-614 2.65e-13

nucleotide-binding domain (NBD) of Bacillus subtilis glucokinase (GLK) and similar proteins; Glucokinase (EC 2.7.1.2), also called glucose kinase, acts as an ATP-dependent kinase that phosphorylates glucose using ATP as a donor to give glucose-6-phosphate and ADP. It is highly specific for glucose. Glucokinases are found in invertebrates and microorganisms. They belong to the kinase (ROK) family, a group of proteins that have sugar kinase and/or transcriptional repressor activities.


Pssm-ID: 466912 [Multi-domain]  Cd Length: 311  Bit Score: 71.17  E-value: 2.65e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298566312 474 GGIIHQHELIHGSSFCAAELGHL-VVSLDGPDCSCGSHGCIEAYASGMALQREAKKLHDEDLLLVEGMSVPKDEAVGALH 552
Cdd:cd24062  141 GGVIANGKIVHGANGAAGEIGHItVNPEGGAPCNCGKTGCLETVASATGIVRIAREELEEGKGSSALRILALGGELTAKD 220

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 298566312 553 LIQAAKLGNAKAQSILRTAGTALGLGVVNILHTMNPSLVILSGVLA---SHYIHIVKDVIRQQAL 614
Cdd:cd24062  221 VFEAAKAGDELALAVVDTVARYLGLALANLANTLNPEKIVIGGGVSaagEFLLSPVKEYFDRFTF 285
ASKHA_ATPase_ROK_Mlc cd24074
ATPase-like domain of protein Mlc and similar proteins; Mlc, also called making large colonies ...
 482-614 1.33e-12

ATPase-like domain of protein Mlc and similar proteins; Mlc, also called making large colonies protein, acts as a transcriptional repressor that regulates the expression of proteins that are part of the phosphotransferase system for sugar uptake. It regulates the expression of malT. Members of this subfamily belong to the kinase (ROK) family, a group of proteins that have sugar kinase and/or transcriptional repressor activities.


Pssm-ID: 466924 [Multi-domain]  Cd Length: 322  Bit Score: 69.26  E-value: 1.33e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298566312 482 LIHGSSFCAAELGHLVVSLDGPDCSCGSHGCIEAYASGMALQREAKKL---HDEDLLLVEGMSVPkdeavgalHLIQAAK 558
Cdd:cd24074  150 LLHAGSSRLGELGHTQIDPYGKRCYCGNHGCLETVASIPAILEQANQLleqSPDSMLHGQPISIE--------SLCQAAL 221

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 298566312 559 LGNAKAQSILRTAGTALGLGVVNILHTMNPSLVILSGVL---ASHYIHIVKDVIRQQAL 614
Cdd:cd24074  222 AGDPLAQDIIIQVGRHLGRILAILVNLFNPEKILIGSPLnnaAEILFPALSQSIRQQSL 280
ASKHA_ATPase_ROK_NagC cd24075
ATPase-like domain of N-acetylglucosamine repressor (NagC) and similar proteins; NagC acts as ...
 481-614 2.07e-12

ATPase-like domain of N-acetylglucosamine repressor (NagC) and similar proteins; NagC acts as a repressor of the nagEBACD operon involved in the uptake and degradation of the amino sugars, N-acetyl-D-glucosamine (GlcNAc) and glucosamine (GlcN). It acts both as an activator and a repressor for the transcription of the glmSU operon, encoding proteins necessary for the synthesis of GlcN (glmS) and the formation of UDP-GlcNAc (glmU). Members of this subfamily belong to the kinase (ROK) family, a group of proteins that have sugar kinase and/or transcriptional repressor activities.


Pssm-ID: 466925 [Multi-domain]  Cd Length: 315  Bit Score: 68.55  E-value: 2.07e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298566312 481 ELIHGSSFCAAELGHLVVSLDGPDCSCGSHGCIEAYASGMALQREAKKLHDEDllLVEGMSvPKDEAVGAlhLIQAAKLG 560
Cdd:cd24075  148 KLFLGQNGNAGEIGHIQIEPLGERCHCGNFGCLETVASNAAIEQRVKKLLKQG--YASQLT-LQDCTIKD--ICQAALNG 222

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 298566312 561 NAKAQSILRTAGTALGLGVVNILHTMNPSLVILSG--VLASHYIH-IVKDVIRQQAL 614
Cdd:cd24075  223 DQLAQDVIKRAGRYLGKVIAILINLLNPQKIIIAGeiTQADKVLLpVIKKCIQSQAL 279
ASKHA_ATPase_ROK_SaXylR-like cd24077
ATPase-like domain of Staphylococcus aureus xylose repressor (XylR) and similar proteins; This ...
 480-612 1.80e-11

ATPase-like domain of Staphylococcus aureus xylose repressor (XylR) and similar proteins; This subfamily includes a group of uncharacterized proteins similar to Staphylococcus aureus xylose repressor (SaXylR), which belongs to the kinase (ROK) family, a group of proteins that have sugar kinase and/or transcriptional repressor activities. SaXylR acts as a transcriptional repressor of xylose-utilizing enzymes. It lacks the cysteine-rich zinc-binding motif, which presents in other family members.


Pssm-ID: 466927 [Multi-domain]  Cd Length: 295  Bit Score: 65.25  E-value: 1.80e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298566312 480 HELIHGSSFCAAELGHLVVSLDGPDCSCGSHGCIEAYASGMALQREAKKLHDedlllVEGMSVPkdeavgalHLIQAAKL 559
Cdd:cd24077  143 NQLYRGYNGFAGEIGHMIIVPNGKPCPCGNKGCLEQYASEKALLKELSEKKG-----LETLTFD--------DLIQLYNE 209

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 298566312 560 GNAKAQSILRTAGTALGLGVVNILHTMNPSLVILSGVLASHYIHIVKDvIRQQ 612
Cdd:cd24077  210 GDPEALELIDQFIKYLAIGINNIINTFNPEIIIINSSLINEIPELLEK-IKEQ 261
ASKHA_NBD_ROK_AlsK cd24070
nucleotide-binding domain (NBD) of D-allose kinase (AlsK) and similar proteins; AlsK (EC 2.7.1. ...
 480-528 4.05e-09

nucleotide-binding domain (NBD) of D-allose kinase (AlsK) and similar proteins; AlsK (EC 2.7.1.55), also called allokinase, catalyzes the phosphorylation of D-allose to D-allose 6-phosphate. It has also low level glucokinase activity in vitro. Members of this subfamily belong to the kinase (ROK) family, a group of proteins that have sugar kinase and/or transcriptional repressor activities.


Pssm-ID: 466920 [Multi-domain]  Cd Length: 293  Bit Score: 58.33  E-value: 4.05e-09
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 298566312 480 HELIHGSSFCAAELGHLVVSLDGPDCSCGSHGCIEAYASGMALQREAKK 528
Cdd:cd24070  146 GKPLRGKNGVAGELGHIPVYGNGKPCGCGNTGCLETYASGRALEEIAEE 194
ASKHA_NBD_ROK_EcFRK-like cd24066
nucleotide-binding domain (NBD) of Escherichia coli fructokinase (FRK) and similar proteins; ...
 481-595 4.12e-09

nucleotide-binding domain (NBD) of Escherichia coli fructokinase (FRK) and similar proteins; Escherichia coli FRK (EC 2.7.1.4), also called D-fructose kinase, manno(fructo)kinase, or MAK, catalyzes the phosphorylation of fructose to fructose-6-phosphate. It has also low level glucokinase activity in vitro. It is not able to phosphorylate D-ribose, D-mannitol, D-sorbitol, inositol, and L-threonine. Members of this subfamily belong to the kinase (ROK) family, a group of proteins that have sugar kinase and/or transcriptional repressor activities.


Pssm-ID: 466916 [Multi-domain]  Cd Length: 294  Bit Score: 58.37  E-value: 4.12e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298566312 481 ELIHGSSFCAAELGHLVV------SLDGPDCSCGSHGCIEAYASGMALQREAKKLHDEDLllvegmsvpkdeavGALHLI 554
Cdd:cd24066  142 RVLTGANGIAGEWGHNPLpwpdedELPGPPCYCGKRGCVETFLSGPALERDYARLTGKTL--------------SAEEIV 207

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 298566312 555 QAAKLGNAKAQSILRTAGTALGLGVVNILHTMNPSLVILSG 595
Cdd:cd24066  208 ALARAGDAAAVATLDRFLDRLGRALANVINILDPDVIVLGG 248
ASKHA_NBD_ROK_EcNanK-like cd24069
nucleotide-binding domain (NBD) of Escherichia coli N-acetylmannosamine kinase and similar ...
 481-606 4.75e-09

nucleotide-binding domain (NBD) of Escherichia coli N-acetylmannosamine kinase and similar proteins; N-acetylmannosamine kinase (NanK; EC 2.7.1.60), also called ManNAc kinase, or N-acetyl-D-mannosamine kinase, catalyzes the phosphorylation of N-acetylmannosamine (ManNAc) to ManNAc-6-P. It has also low level glucokinase activity in vitro. This subfamily also contains Brucella melitensis bifunctional enzyme NanE/NanK (EC 5.1.3.9/EC 2.7.1.60), which also converts N-acetylmannosamine-6-phosphate (ManNAc-6-P) to N-acetylglucosamine-6-phosphate (GlcNAc-6-P). Members of this subfamily belong to the kinase (ROK) family, a group of proteins that have sugar kinase and/or transcriptional repressor activities.


Pssm-ID: 466919 [Multi-domain]  Cd Length: 283  Bit Score: 58.06  E-value: 4.75e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298566312 481 ELIHGSSFCAAELGHLVVSLDGPDCSCGSHGCIEAYASGMALQREAkklhdedlllvegmSVPKDEAVGALHLIQAAKLG 560
Cdd:cd24069  139 QLLTGPNGLAGHIGHTLADPPGPVCGCGRRGCVEAIASGTAIAAAA--------------SEILGEPVDAKDVFERARSG 204

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 298566312 561 NAKAQSILRTAGTALGLGVVNILHTMNPSLVILSGV--LASHYIHIVK 606
Cdd:cd24069  205 DEEAARLIDRAARALADLIADLKATLDLDCVVIGGSvgLAEGFLERVE 252
PRK05082 PRK05082
N-acetylmannosamine kinase; Provisional
 479-612 3.44e-08

N-acetylmannosamine kinase; Provisional


Pssm-ID: 235338 [Multi-domain]  Cd Length: 291  Bit Score: 55.30  E-value: 3.44e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298566312 479 QHELIHGSSFCAAELGHLVVSLDGPDCSCGSHGCIEAYASGMALQREAKKLhdedlllvegmsvpKDEAVGALHLIQAAK 558
Cdd:PRK05082 140 NGKLLTGPGGLAGHIGHTLADPHGPVCGCGRRGCVEAIASGRAIAAAAQGW--------------LAGCDAKTIFERAGQ 205

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 298566312 559 lGNAKAQSILRTAGTALGLGVVNILHTMNPSLVILSGV--LASHYIHIVKDVIRQQ 612
Cdd:PRK05082 206 -GDEQAQALINRSAQAIARLIADLKATLDCQCVVLGGSvgLAEGYLELVQAYLAQE 260
ASKHA_NBD_ROK_NAGK cd24057
nucleotide-binding domain (NBD) of N-acetyl-D-glucosamine kinase (NAGK) and similar proteins; ...
 473-598 3.30e-06

nucleotide-binding domain (NBD) of N-acetyl-D-glucosamine kinase (NAGK) and similar proteins; NAGK (EC 2.7.1.59), also called GlcNAc kinase, catalyzes the phosphorylation of N-acetyl-D-glucosamine (GlcNAc) derived from cell-wall degradation, yielding GlcNAc-6-P. Members of this subfamily belong to the kinase (ROK) family, a group of proteins that have sugar kinase and/or transcriptional repressor activities.


Pssm-ID: 466907 [Multi-domain]  Cd Length: 298  Bit Score: 49.15  E-value: 3.30e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298566312 473 GGGIIHQHELIHGSSFCAAELGHLVVSLD----GPD-----CSCGSHGCIEAYASGMALQREAKKLHDEDLllvegmsvp 543
Cdd:cd24057  135 GGGLVVNGRLVGGRSGIAGEWGHGPLPADalllGYDlpvlrCGCGQTGCLETYLSGRGLERLYAHLYGEEL--------- 205

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 298566312 544 kdeavGALHLIQAAKLGNAKAQSILRTAGTALGLGVVNILHTMNPSLVILSGVLA 598
Cdd:cd24057  206 -----DAPEIIAAWAAGDPQAVAHVDRWLDLLAGCLANILTALDPDVVVLGGGLS 255
PRK09698 PRK09698
D-allose kinase; Provisional
 482-528 4.47e-06

D-allose kinase; Provisional


Pssm-ID: 182034 [Multi-domain]  Cd Length: 302  Bit Score: 48.83  E-value: 4.47e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 298566312 482 LIHGSSFCAAELGHLVVSLDGPDCSCGSHGCIEAYASGMALQREAKK 528
Cdd:PRK09698 151 PWTGAHGVAGELGHIPLGDMTQHCGCGNPGCLETNCSGMALRRWYEQ 197
ASKHA_ATPase_ROK cd23763
ATPase-like domain of the ROK (Repressor, ORF, Kinase) domain family; The ROK family ...
 567-610 8.56e-05

ATPase-like domain of the ROK (Repressor, ORF, Kinase) domain family; The ROK family corresponds to a group of proteins including sugar kinases, transcriptional repressors, and yet uncharacterized open reading frames. ROK family sugar kinases phosphorylate a range of structurally distinct hexoses including the key carbon source D-glucose, various glucose epimers, and several acetylated hexosamines. The sugar kinases include N-acetyl-D-glucosamine kinase (NAGK; EC 2.7.1.59), polyphosphate glucokinase (PPGK; EC 2.7.1.63/EC 2.7.1.2), glucokinase (GLK; EC 2.7.1.2), fructokinase (FRK; EC 2.7.1.4), hexokinase (HK; EC 2.7.1.1), D-allose kinase (AlsK; EC 2.7.1.55), bifunctional UDP-N-acetylglucosamine 2-epimerase/N-acetylmannosamine kinase (GNE; EC 3.2.1.183/EC 2.7.1.60), N-acetylmannosamine kinase (NanK; EC 2.7.1.60), beta-glucoside kinase (BglK; EC 2.7.1.85), and N-acetylglucosamine kinase (EC 2.7.1.59). The family also contains the repressor proteins, such as N-acetylglucosamine repressor (NagC), xylose repressor (XylR), cyclobis-(1-6)-alpha-nigerosyl repressor (CYANR) and protein Mlc. ROK kinases harbor a conserved N-terminal ATP binding motif of sequence DxGxT, while ROK repressors possess a N-terminal extension that contains a canonical helix-turn-helix DNA binding motif. The ROK family proteins belong to the ASKHA (Acetate and Sugar Kinases/Hsc70/Actin) superfamily of phosphotransferases, all members of which share a common characteristic five-stranded beta sheet occurring in both the N- and C-terminal domains.


Pssm-ID: 466849 [Multi-domain]  Cd Length: 239  Bit Score: 44.38  E-value: 8.56e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 298566312 567 ILRTAGTALGLGVVNILHTMNPSLVILSGVLASHYIHIVKDVIR 610
Cdd:cd23763  163 VLEEAARYLGIGLANLINLLNPELIVLGGGVAEAGDLLLEPIRE 206
ASKHA_ATPase_ROK cd23763
ATPase-like domain of the ROK (Repressor, ORF, Kinase) domain family; The ROK family ...
 410-460 4.98e-04

ATPase-like domain of the ROK (Repressor, ORF, Kinase) domain family; The ROK family corresponds to a group of proteins including sugar kinases, transcriptional repressors, and yet uncharacterized open reading frames. ROK family sugar kinases phosphorylate a range of structurally distinct hexoses including the key carbon source D-glucose, various glucose epimers, and several acetylated hexosamines. The sugar kinases include N-acetyl-D-glucosamine kinase (NAGK; EC 2.7.1.59), polyphosphate glucokinase (PPGK; EC 2.7.1.63/EC 2.7.1.2), glucokinase (GLK; EC 2.7.1.2), fructokinase (FRK; EC 2.7.1.4), hexokinase (HK; EC 2.7.1.1), D-allose kinase (AlsK; EC 2.7.1.55), bifunctional UDP-N-acetylglucosamine 2-epimerase/N-acetylmannosamine kinase (GNE; EC 3.2.1.183/EC 2.7.1.60), N-acetylmannosamine kinase (NanK; EC 2.7.1.60), beta-glucoside kinase (BglK; EC 2.7.1.85), and N-acetylglucosamine kinase (EC 2.7.1.59). The family also contains the repressor proteins, such as N-acetylglucosamine repressor (NagC), xylose repressor (XylR), cyclobis-(1-6)-alpha-nigerosyl repressor (CYANR) and protein Mlc. ROK kinases harbor a conserved N-terminal ATP binding motif of sequence DxGxT, while ROK repressors possess a N-terminal extension that contains a canonical helix-turn-helix DNA binding motif. The ROK family proteins belong to the ASKHA (Acetate and Sugar Kinases/Hsc70/Actin) superfamily of phosphotransferases, all members of which share a common characteristic five-stranded beta sheet occurring in both the N- and C-terminal domains.


Pssm-ID: 466849 [Multi-domain]  Cd Length: 239  Bit Score: 42.07  E-value: 4.98e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 298566312 410 LAVDLGGTNLRVAIVSMKGEIVKKYTQFNP--KTYEERINLILQMCVEAAAEA 460
Cdd:cd23763    1 IGIDIGGTKIRAALVDLDGEILARERVPTPaeEGPEAVLDRIAELIEELLAEA 53
PRK13310 PRK13310
N-acetyl-D-glucosamine kinase; Provisional
 473-604 8.43e-04

N-acetyl-D-glucosamine kinase; Provisional


Pssm-ID: 183967 [Multi-domain]  Cd Length: 303  Bit Score: 41.90  E-value: 8.43e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298566312 473 GGGIIHQHELIHGSSFCAAELGHL--------VVSLDGP--DCSCGSHGCIEAYASGMALQreakklhdedlLLVEGMsv 542
Cdd:PRK13310 135 GGGLVFNGKPISGRSYITGEFGHMrlpvdaltLLGWDAPlrRCGCGQKGCIENYLSGRGFE-----------WLYQHY-- 201

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 298566312 543 pKDEAVGALHLIQAAKLGNAKAQSILRTAGTALGLGVVNILHTMNPSLVILSGVLaSHYIHI 604
Cdd:PRK13310 202 -YGEPLQAPEIIALYYQGDEQAVAHVERYLDLLAICLGNILTIVDPHLVVLGGGL-SNFDAI 261
ASKHA_NBD_HK cd24000
nucleotide-binding domain (NBD) of the hexokinase (HK) domain family; Hexokinase (EC 2.7.1.1) ...
 396-429 2.29e-03

nucleotide-binding domain (NBD) of the hexokinase (HK) domain family; Hexokinase (EC 2.7.1.1) possesses the ability to transfer an inorganic phosphate group from ATP to a substrate. It catalyzes the ATP-dependent phosphorylation of aldo- and keto-hexose sugars to the hexose-6-phosphate (H6P). It can catalyze this reaction on glucose, fructose, sorbitol and glucosamine, and as such is the first step in a number of metabolic pathways. Hexokinase contains two structurally similar domains. Some members of the family have two copies of each of these domains. Hexokinases belong to the ASKHA (Acetate and Sugar Kinases/Hsc70/Actin) superfamily of phosphotransferases, all members of which share a common characteristic five-stranded beta sheet occurring in both the N- and C-terminal domains.


Pssm-ID: 466850 [Multi-domain]  Cd Length: 357  Bit Score: 40.72  E-value: 2.29e-03
                         10        20        30
                 ....*....|....*....|....*....|....
gi 298566312 396 ISQDIDHiLETLSALAVDLGGTNLRVAIVSMKGE 429
Cdd:cd24000   33 VSPLPTG-LESGEFLAIDLGGTNLRVALVSLDGK 65
ASKHA_NBD_HK1-2_fungi cd24087
nucleotide-binding domain (NBD) of hexokinase isozymes PI and PII from fungal hexokinase (HK) ...
 405-429 3.72e-03

nucleotide-binding domain (NBD) of hexokinase isozymes PI and PII from fungal hexokinase (HK) domain family; Hexokinase (EC 2.7.1.1) possesses the ability to transfer an inorganic phosphate group from ATP to a substrate. It catalyzes the ATP-dependent phosphorylation of aldo- and keto-hexose sugars to the hexose-6-phosphate (H6P). It can catalyze this reaction on glucose, fructose, sorbitol and glucosamine, and as such is the first step in a number of metabolic pathways. Hexokinase contains two structurally similar domains. Some members of the family have two copies of each of these domains. There are three isozymes of hexokinase in yeast (PI, PII and glucokinase): isozymes PI and PII phosphorylate both aldo- and keto-sugars; glucokinase (EC 2.7.1.2) is specific for aldo-hexoses. Early meiotic induction protein 2 (EMI2, also known as glucokinase-2, EC 2.7.1.2) might be another isozyme of hexokinase in yeast. Yeast hexokinases reveal a well-defined catalytic pocket that binds ATP and hexose, allowing easy transfer of the phosphate from ATP to the sugar. The family corresponds to hexokinase PI and PII, which are also known as hexokinase-1/hexokinase-A and hexokinase-2/hexokinase-B, respectively.


Pssm-ID: 466937 [Multi-domain]  Cd Length: 428  Bit Score: 40.05  E-value: 3.72e-03
                         10        20
                 ....*....|....*....|....*
gi 298566312 405 ETLSALAVDLGGTNLRVAIVSMKGE 429
Cdd:cd24087   41 ETGDYLALDLGGTNLRVCLVKLGGN 65
Hexokinase_1 pfam00349
Hexokinase; Hexokinase (EC:2.7.1.1) contains two structurally similar domains represented by ...
 410-436 9.46e-03

Hexokinase; Hexokinase (EC:2.7.1.1) contains two structurally similar domains represented by this family and pfam03727. Some members of the family have two copies of each of these domains.


Pssm-ID: 459774 [Multi-domain]  Cd Length: 197  Bit Score: 37.87  E-value: 9.46e-03
                          10        20
                  ....*....|....*....|....*..
gi 298566312  410 LAVDLGGTNLRVAIVSMKGEIVKKYTQ 436
Cdd:pfam00349  59 LALDLGGTNFRVCLVELGGDGKFEITQ 85
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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